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Database: UniProt
Entry: K1MCB1_9LACT
LinkDB: K1MCB1_9LACT
Original site: K1MCB1_9LACT 
ID   K1MCB1_9LACT            Unreviewed;       358 AA.
AC   K1MCB1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Glutamyl aminopeptidase {ECO:0000313|EMBL:EKB53669.1};
GN   ORFNames=HMPREF9707_01422 {ECO:0000313|EMBL:EKB53669.1};
OS   Falseniella ignava CCUG 37419.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Falseniella.
OX   NCBI_TaxID=883112 {ECO:0000313|EMBL:EKB53669.1, ECO:0000313|Proteomes:UP000005147};
RN   [1] {ECO:0000313|EMBL:EKB53669.1, ECO:0000313|Proteomes:UP000005147}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 37419 {ECO:0000313|EMBL:EKB53669.1,
RC   ECO:0000313|Proteomes:UP000005147};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Facklamia ignava CCUG 37419.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000256|PIRSR:PIRSR001123-2};
CC   -!- SIMILARITY: Belongs to the peptidase M42 family.
CC       {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKB53669.1}.
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DR   EMBL; AGZE01000037; EKB53669.1; -; Genomic_DNA.
DR   RefSeq; WP_006702057.1; NZ_JH932301.1.
DR   AlphaFoldDB; K1MCB1; -.
DR   STRING; 883112.HMPREF9707_01422; -.
DR   PATRIC; fig|883112.3.peg.1418; -.
DR   eggNOG; COG1363; Bacteria.
DR   HOGENOM; CLU_047249_0_2_9; -.
DR   Proteomes; UP000005147; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05656; M42_Frv; 1.
DR   Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017538; Pept_M42_glutamyl_aminopept.
DR   InterPro; IPR008007; Peptidase_M42.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   NCBIfam; TIGR03107; glu_aminopep; 1.
DR   PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR32481:SF0; AMINOPEPTIDASE YPDE-RELATED; 1.
DR   Pfam; PF05343; Peptidase_M42; 1.
DR   PIRSF; PIRSF001123; PepA_GA; 1.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:EKB53669.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005147}.
FT   ACT_SITE        213
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ   SEQUENCE   358 AA;  39374 MW;  E0B7A248AF86315A CRC64;
     MSDKLFQRIK ELTELQGISG YERNVRQYLV EHMTPLVDEI EVSDLGNVYG IIRSKQQNAP
     KVMIAAHMDE VGFMVTEIHN NGTMSVTPIG GWNVYAVSAQ RYTLQTAKGD YPIVSSAVAP
     HLLRGGGQAA SLKPEDIRFD AGFDSKEEAE SYGVRPGNAI VPEVETIYAA NGKNLIGKSW
     DNRYGCVAIL DLLEYVQGKE LDCDLIIGAN VQEEVGLRGV RGAVTRYQPD VFIAVDCSPA
     GDSESSTGVQ GRLGEGFLLR MQDPGMLTHR GLIDYFVETA ERHEIDYQYF FSKGGTDAGA
     AHTMNEGIIS GVIGVPARYI HGHQSIYRLS DYKAAIAMLQ QVVTEFNVET LKTIRENN
//
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